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Does Tetracycline Bind Helix 2 Of Prion? An Integrated Spectroscopical And Computational Study Of The Interaction Between The Antibiotic And Alpha Helix 2 Human Prion Protein Fragments (83 views)

Ronga L, Langella E, Palladino P, Marasco D, Tizzano B, Saviano M, Pedone C, Improta R, Ruvo M

Proteins (ISSN: 0887-3585, 1097-0134, 1097-0134electronic), 2007 Feb 15; 66(3): 707-715.

Abstract
We demonstrate here that tetracycline (TC) can strongly interact (K-D = 189 +/- 7 nM) with model peptides derived from the C-terminal globular domain of the prion protein, hPrP [173-195], and that interaction concerns residues within the C-terminal half of the helix 2, a short region previously indicated as endowed with ambivalent conformational behavior and implicated in PrP conversion to the P-sheet-rich, infective scrapie variant. Data have been confirmed by binding studies with the N-terminal truncated 180-195 variant that displays a dissociation constant of 483 +/- 30 nM. Remarkably, TC does not influence the structure of the N-terminally fluoresceinated peptides that both show alpha-helical conformations. Docking calculations and molecular dynamics simulations suggest a direct, strong interaction of the antibiotic with exposed side chain functional groups of threonines 190-193 on the solvent-exposed surface of helix 2. Proteins 2007; 66: 707-715. (c) 2006 Wiley-Liss, Inc

Affiliations ▼
*** IBB - CNR Affiliation

Istituto di Biostrutture e Bioimmagini del CNR, Sezione Biostrutture, via Mezzocannone 16, 80134 Napoli, Italy

Dipartimento delle Scienze Biologiche, Sezione Biostrutture, Università Federico II, via Mezzocannone, 16, 80134 Napoli, Italy

Details ▼
Impact factor: 3.354, 5-year impact factor: 3.905

Paper type: Journal Article, Research Support, Non-U. S. Gov'T,

Keywords: Cd Spectroscopy, Docking Calculations, Fluorescence Spectroscopy, Molecular Dynamics, Prion Peptides, Tetracycline, Antibiotic Agent, Prion Protein, Solvent, Threonine, Alpha Helix, Amino Terminal Sequence, Antibiotic Therapy, Beta Sheet, Carboxy Terminal Sequence, Conference Paper, Dissociation Constant, Drug Protein Binding, Human, Mathematical Computing, Priority Journal, Protein Conformation, Protein Interaction, Solvent Effect, Amino Acid Sequence, Anti-Bacterial Agents, Circular Dichroism, Kinetics, Molecular Sequence Data, Spectrometry,

Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-33846202560&partnerID=40&md5=c035398b7f05be92579f3b9e038ab62a

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Abramov, A. Y., Canevari, L., Duchen, M. R., Calcium signals induced by amyloid beta peptide and their consequences in neurons and astrocytes in culture (2004) Biochim Biophys Acta, 6, pp. 81-87

Othersen, O. G., Beierlein, F., Lanig, H., Clark, T., Conformations and tautomers of tetracycline (2003) J Phys Chem B, 107, pp. 13743-13749

Morris, G. M., Goodsell, D. S., Halliday, R. S., Huey, R., Hart, W. E., Belew, R. K., Olson, A. J., Automated docking using a Lamarckian genetic algorithm and empirical binding free energy function (1998) J Comput Chem, 19, pp. 1639-1662

Berendsen, H. J. C., Postma, J. P. M., van Gunsteren, W. F., Hermans, J., (1981) Intermolecular Forces, pp. 331-342. , Pullman, B, editor, Dordrecht, The Netherlands: Reidel

1986van Buuren, A. R. S., Marrink, J., Berendsen, H. J. C., A molecular dynamics study of the decane/water interface (1993) J Phys Chem, 97, pp. 9206-9212

D'Ursi, A. M., Arenante, M. R., Guerrini, R., Salvatori, S., Sorrentino, G., Picone, D., Solution structure of amyloid -peptide 25-35 in different media (2004) J Med Chem, 47, pp. 4231-4238

Dima, R. I., Thirumalai, D., Probing the instabilities in the dynamics of helical fragments from mouse PrPC (2004) Proc Natl Acad Sci USA, 101, pp. 15335-15340

Shamsir, M. S., Dalby, A. R., One gene two diseases and three conformations: Molecular dynamics simulations of mutants of human prion protein at room temperature and elevated temperatures. Proteins: Struct Funct (2005) Bioinform, 59, pp. 72-79


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1 Records (1 excluding Abstracts and Conferences).
Total impact factor: 1.849 (1.849 excluding Abstracts and Conferences).
Total 5-year impact factor: 1.45 (1.45 excluding Abstracts and Conferences).



Your bibliography query: (([btitle, keywords, abstract] SPECTROSCOPY AND [btitle, keywords, abstract] DOCKING AND [btitle, keywords, abstract] CALCULATIONS)) AND NOT [id] = 50961



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